Characterization and immunogenicity of norovirus capsid-derived virus-like particles purified by anion exchange chromatography

Recombinant baculovirus (BV) expression systems are widely applied in the production of viral capsid proteins and virus-like particles (VLPs) for use as immunogens and vaccine candidates. Traditional density gradient purification of VLPs does not enable complete elimination of BV-derived impurities,...

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Detalles Bibliográficos
Autores principales: Huhti, L., Tamminen, K., Vesikari, T., Blazevic, V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Vienna 2012
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7087179/
https://www.ncbi.nlm.nih.gov/pubmed/23229011
http://dx.doi.org/10.1007/s00705-012-1565-7
Descripción
Sumario:Recombinant baculovirus (BV) expression systems are widely applied in the production of viral capsid proteins and virus-like particles (VLPs) for use as immunogens and vaccine candidates. Traditional density gradient purification of VLPs does not enable complete elimination of BV-derived impurities, including live viruses, envelope glycoprotein gp64 and baculoviral DNA. We used an additional purification system based on ionic strength to purify norovirus (NoV) GII-4 capsid-derived VLPs. The anion exchange chromatography purification led to highly purified VLPs free from BV impurities with intact morphology. In addition, highly purified VLPs induced strong NoV-specific antibody responses in BALB/c mice. Here, we describe a method for NoV VLP purification and several methods for determining their purity, including quantitative PCR for BV DNA detection.

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